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Database: PDB
Entry: 4USE
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Original site: 4USE 
HEADER    TRANSFERASE                             07-JUL-14   4USE              
TITLE     HUMAN STK10 (LOK) WITH SB-633825                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE 10;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: KINASE DOMAIN, RESIDUES 18-317;                            
COMPND   5 SYNONYM: LYMPHOCYTE-ORIENTED KINASE, STK10;                          
COMPND   6 EC: 2.7.11.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.ELKINS,E.SALAH,M.SZKLARZ,F.VON DELFT,P.CANNING,J.RAYNOR,          
AUTHOR   2 C.BOUNTRA,A.M.EDWARDS,S.KNAPP                                        
REVDAT   4   24-JAN-18 4USE    1       AUTHOR                                   
REVDAT   3   20-JAN-16 4USE    1       JRNL                                     
REVDAT   2   04-NOV-15 4USE    1       JRNL                                     
REVDAT   1   22-JUL-15 4USE    0                                                
JRNL        AUTH   J.M.ELKINS,V.FEDELE,M.SZKLARZ,K.R.ABDUL AZEEZ,E.SALAH,       
JRNL        AUTH 2 J.MIKOLAJCZYK,S.ROMANOV,N.SEPETOV,X.P.HUANG,B.L.ROTH,        
JRNL        AUTH 3 A.AL HAJ ZEN,D.FOURCHES,E.MURATOV,A.TROPSHA,J.MORRIS,        
JRNL        AUTH 4 B.A.TEICHER,M.KUNKEL,E.POLLEY,K.E.LACKEY,F.L.ATKINSON,       
JRNL        AUTH 5 J.P.OVERINGTON,P.BAMBOROUGH,S.MOLLER,D.J.PRICE,T.M.WILLSON,  
JRNL        AUTH 6 D.H.DREWRY,S.KNAPP,W.J.ZUERCHER                              
JRNL        TITL   COMPREHENSIVE CHARACTERIZATION OF THE PUBLISHED KINASE       
JRNL        TITL 2 INHIBITOR SET.                                               
JRNL        REF    NAT.BIOTECHNOL.               V.  34    95 2016              
JRNL        REFN                   ISSN 1087-0156                               
JRNL        PMID   26501955                                                     
JRNL        DOI    10.1038/NBT.3374                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 131.18                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 22179                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.226                           
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1192                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.72                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1486                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.81                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3740                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 83                           
REMARK   3   BIN FREE R VALUE                    : 0.4020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4284                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 70                                      
REMARK   3   SOLVENT ATOMS            : 16                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 72.11                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.08000                                              
REMARK   3    B22 (A**2) : -3.11000                                             
REMARK   3    B33 (A**2) : -1.92000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.79000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.591         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.304         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.306         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 33.069        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4461 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4241 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6087 ; 1.268 ; 1.995       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9737 ; 0.826 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   560 ; 6.096 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   167 ;35.837 ;24.850       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   726 ;16.477 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;18.630 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   706 ; 0.068 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4944 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   916 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2252 ; 1.624 ; 3.504       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2251 ; 1.619 ; 3.504       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2805 ; 2.853 ; 5.252       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2209 ; 2.135 ; 3.731       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    30        A   112                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.8204   0.7536 -55.1176              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4578 T22:   0.7251                                     
REMARK   3      T33:   0.4108 T12:   0.0827                                     
REMARK   3      T13:   0.0896 T23:   0.1337                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.7604 L22:   2.2377                                     
REMARK   3      L33:   1.8562 L12:   2.1195                                     
REMARK   3      L13:  -1.9977 L23:   1.0717                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0169 S12:  -0.3354 S13:  -0.5461                       
REMARK   3      S21:   0.4527 S22:  -0.5116 S23:   0.4720                       
REMARK   3      S31:   0.2360 S32:  -0.6208 S33:   0.4947                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   113        A   188                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.4832   0.0822 -55.1678              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1247 T22:   0.0142                                     
REMARK   3      T33:   0.0499 T12:  -0.0263                                     
REMARK   3      T13:   0.0305 T23:  -0.0168                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6056 L22:   7.1459                                     
REMARK   3      L33:   4.6006 L12:  -1.4545                                     
REMARK   3      L13:   1.3995 L23:   1.5860                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0806 S12:  -0.0783 S13:   0.0485                       
REMARK   3      S21:   0.2436 S22:  -0.0629 S23:   0.5062                       
REMARK   3      S31:   0.0083 S32:   0.0387 S33:   0.1435                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   189        A   216                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.6311   7.0807 -40.4548              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9614 T22:   0.6291                                     
REMARK   3      T33:   0.4175 T12:  -0.2339                                     
REMARK   3      T13:  -0.0804 T23:  -0.0460                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8460 L22:   4.8494                                     
REMARK   3      L33:  16.6370 L12:   1.7321                                     
REMARK   3      L13:   2.7595 L23:   8.7738                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4723 S12:   0.0997 S13:   0.2292                       
REMARK   3      S21:   1.3504 S22:  -0.3226 S23:   0.0274                       
REMARK   3      S31:   2.5002 S32:  -1.1790 S33:  -0.1497                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   217        A   316                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.2036  -0.0683 -47.9762              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1110 T22:   0.1253                                     
REMARK   3      T33:   0.0519 T12:   0.0063                                     
REMARK   3      T13:  -0.0257 T23:  -0.0180                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9177 L22:   5.2683                                     
REMARK   3      L33:   5.0611 L12:   0.5370                                     
REMARK   3      L13:   0.6399 L23:   1.7554                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0375 S12:  -0.2040 S13:   0.0842                       
REMARK   3      S21:   0.4851 S22:   0.1182 S23:  -0.4316                       
REMARK   3      S31:   0.0079 S32:   0.6369 S33:  -0.0807                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    34        B    89                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.5477 -20.5790 -18.3488              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1032 T22:   1.2629                                     
REMARK   3      T33:   1.1729 T12:   0.0401                                     
REMARK   3      T13:   0.1387 T23:   0.3564                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6212 L22:   6.5776                                     
REMARK   3      L33:   5.2812 L12:   1.5415                                     
REMARK   3      L13:   1.2351 L23:   5.0427                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1464 S12:   0.3633 S13:   0.6020                       
REMARK   3      S21:  -0.9192 S22:  -0.3619 S23:   1.0555                       
REMARK   3      S31:  -0.6749 S32:  -0.7175 S33:   0.5083                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    90        B   188                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.4957 -21.7311  -9.7021              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5952 T22:   0.0464                                     
REMARK   3      T33:   0.1123 T12:   0.0398                                     
REMARK   3      T13:   0.1223 T23:  -0.0146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2927 L22:   5.5638                                     
REMARK   3      L33:   5.2259 L12:   1.2028                                     
REMARK   3      L13:  -1.9623 L23:   0.0631                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0052 S12:   0.3779 S13:  -0.0394                       
REMARK   3      S21:  -0.0433 S22:  -0.0613 S23:   0.6505                       
REMARK   3      S31:   0.0522 S32:  -0.3394 S33:   0.0561                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   189        B   217                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.7996 -27.4314 -23.6715              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8614 T22:   0.6260                                     
REMARK   3      T33:   0.3811 T12:   0.1841                                     
REMARK   3      T13:   0.1616 T23:  -0.0971                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3232 L22:   6.3844                                     
REMARK   3      L33:  12.4066 L12:  -2.9505                                     
REMARK   3      L13:  -3.4598 L23:   8.7571                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4535 S12:  -0.1627 S13:  -0.2636                       
REMARK   3      S21:  -1.2380 S22:  -0.5990 S23:   0.1371                       
REMARK   3      S31:  -1.6489 S32:  -1.0864 S33:   0.1456                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   218        B   316                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.3369 -20.6843 -12.7668              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4597 T22:   0.1305                                     
REMARK   3      T33:   0.0922 T12:  -0.0047                                     
REMARK   3      T13:   0.0722 T23:  -0.0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4121 L22:   4.9972                                     
REMARK   3      L33:   4.9168 L12:  -0.8729                                     
REMARK   3      L13:  -1.7222 L23:   1.7675                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0723 S12:  -0.1675 S13:  -0.1083                       
REMARK   3      S21:  -0.0404 S22:   0.1564 S23:  -0.5706                       
REMARK   3      S31:  -0.0056 S32:   0.7741 S33:  -0.0841                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 4USE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-JUL-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290061187.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JUL-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PIXEL                      
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23790                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 65.590                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.91000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50% (V/V) PEG 300, 0.1M CACODYLATE PH    
REMARK 280  6.5, 0.2M MGCL2                                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       25.12500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    16                                                      
REMARK 465     MET A    17                                                      
REMARK 465     ARG A    18                                                      
REMARK 465     LYS A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     ARG A    21                                                      
REMARK 465     GLU A    22                                                      
REMARK 465     TYR A    23                                                      
REMARK 465     LYS A   188                                                      
REMARK 465     ARG A   189                                                      
REMARK 465     ASP A   190                                                      
REMARK 465     SER A   191                                                      
REMARK 465     PHE A   192                                                      
REMARK 465     ILE A   193                                                      
REMARK 465     GLY A   194                                                      
REMARK 465     GLU A   317                                                      
REMARK 465     SER B    16                                                      
REMARK 465     MET B    17                                                      
REMARK 465     ARG B    18                                                      
REMARK 465     LYS B    19                                                      
REMARK 465     SER B    20                                                      
REMARK 465     ARG B    21                                                      
REMARK 465     GLU B    22                                                      
REMARK 465     TYR B    23                                                      
REMARK 465     GLU B    68                                                      
REMARK 465     THR B    69                                                      
REMARK 465     LYS B    70                                                      
REMARK 465     SER B    71                                                      
REMARK 465     HIS B   102                                                      
REMARK 465     ASP B   103                                                      
REMARK 465     GLY B   104                                                      
REMARK 465     LYS B   105                                                      
REMARK 465     LEU B   106                                                      
REMARK 465     ARG B   189                                                      
REMARK 465     ASP B   190                                                      
REMARK 465     SER B   191                                                      
REMARK 465     PHE B   192                                                      
REMARK 465     ILE B   193                                                      
REMARK 465     GLY B   194                                                      
REMARK 465     GLU B   317                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  24    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  27    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  28    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A  30    CG   CD1  CD2                                       
REMARK 470     GLU A  34    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  49    CE   NZ                                             
REMARK 470     LYS A  54    CE   NZ                                             
REMARK 470     LYS A  56    CD   CE   NZ                                        
REMARK 470     GLU A  57    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  70    CG   CD   CE   NZ                                   
REMARK 470     GLU A  72    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  73    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  76    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  83    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 105    NZ                                                  
REMARK 470     ARG A 152    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 184    NZ                                                  
REMARK 470     LEU A 186    CG   CD1  CD2                                       
REMARK 470     GLN A 187    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 210    CG   CD   CE   NZ                                   
REMARK 470     ASP A 211    CG   OD1  OD2                                       
REMARK 470     LYS A 251    CD   CE   NZ                                        
REMARK 470     LYS A 272    CE   NZ                                             
REMARK 470     GLU B  24    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  27    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  28    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B  29    CG   OD1  OD2                                       
REMARK 470     LEU B  30    CG   CD1  CD2                                       
REMARK 470     GLU B  34    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  41    CD   OE1  OE2                                       
REMARK 470     PHE B  47    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B  49    CD   CE   NZ                                        
REMARK 470     LYS B  54    CE   NZ                                             
REMARK 470     ASN B  55    CG   OD1  ND2                                       
REMARK 470     LYS B  56    CE   NZ                                             
REMARK 470     GLU B  57    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  72    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  73    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  76    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  77    CG   OD1  OD2                                       
REMARK 470     GLU B  83    CG   CD   OE1  OE2                                  
REMARK 470     TYR B 101    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG B 156    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 181    CE   NZ                                             
REMARK 470     LYS B 184    CE   NZ                                             
REMARK 470     LEU B 186    CG   CD1  CD2                                       
REMARK 470     GLN B 187    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 188    CG   CD   CE   NZ                                   
REMARK 470     LYS B 210    CG   CD   CE   NZ                                   
REMARK 470     LYS B 251    CD   CE   NZ                                        
REMARK 470     LYS B 272    CE   NZ                                             
REMARK 470     LYS B 311    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    THR A   212     N    TYR A   214              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B 152   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  30      107.54     68.62                                   
REMARK 500    LEU A  42      -53.66   -140.06                                   
REMARK 500    ALA A  46      -58.52   -163.88                                   
REMARK 500    SER A  71      140.31     94.74                                   
REMARK 500    GLU A  76      -36.05    -39.44                                   
REMARK 500    ASP A 103     -139.99     66.75                                   
REMARK 500    ASP A 157       36.52   -148.81                                   
REMARK 500    LEU A 183       25.42    -71.76                                   
REMARK 500    PRO A 196       50.84    -97.26                                   
REMARK 500    ASP A 211      -72.73    -86.98                                   
REMARK 500    THR A 212     -131.21   -141.11                                   
REMARK 500    PRO A 213      -24.15    -29.66                                   
REMARK 500    ILE A 233      -42.66     75.94                                   
REMARK 500    LEU B  30      108.93     70.15                                   
REMARK 500    LEU B  42      -53.74   -140.72                                   
REMARK 500    ALA B  46      -57.15   -165.51                                   
REMARK 500    GLU B  57      -70.04    -75.82                                   
REMARK 500    GLU B  76      -35.97    -39.55                                   
REMARK 500    ASP B 157       36.84   -149.12                                   
REMARK 500    PRO B 196       50.90    -96.21                                   
REMARK 500    ASP B 211      -88.52    -65.62                                   
REMARK 500    THR B 212      -19.52   -159.08                                   
REMARK 500    ILE B 233      -42.92     75.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR A  212     PRO A  213                 -147.92                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE R09 A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE R09 B 500                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4USD   RELATED DB: PDB                                   
REMARK 900 HUMAN STK10 (LOK) WITH SB-633825                                     
REMARK 900 RELATED ID: 4USF   RELATED DB: PDB                                   
REMARK 900 HUMAN SLK WITH SB-440719                                             
DBREF  4USE A   18   317  UNP    O94804   STK10_HUMAN     18    317             
DBREF  4USE B   18   317  UNP    O94804   STK10_HUMAN     18    317             
SEQADV 4USE SER A   16  UNP  O94804              EXPRESSION TAG                 
SEQADV 4USE MET A   17  UNP  O94804              EXPRESSION TAG                 
SEQADV 4USE SER B   16  UNP  O94804              EXPRESSION TAG                 
SEQADV 4USE MET B   17  UNP  O94804              EXPRESSION TAG                 
SEQRES   1 A  302  SER MET ARG LYS SER ARG GLU TYR GLU HIS VAL ARG ARG          
SEQRES   2 A  302  ASP LEU ASP PRO ASN GLU VAL TRP GLU ILE VAL GLY GLU          
SEQRES   3 A  302  LEU GLY ASP GLY ALA PHE GLY LYS VAL TYR LYS ALA LYS          
SEQRES   4 A  302  ASN LYS GLU THR GLY ALA LEU ALA ALA ALA LYS VAL ILE          
SEQRES   5 A  302  GLU THR LYS SER GLU GLU GLU LEU GLU ASP TYR ILE VAL          
SEQRES   6 A  302  GLU ILE GLU ILE LEU ALA THR CYS ASP HIS PRO TYR ILE          
SEQRES   7 A  302  VAL LYS LEU LEU GLY ALA TYR TYR HIS ASP GLY LYS LEU          
SEQRES   8 A  302  TRP ILE MET ILE GLU PHE CYS PRO GLY GLY ALA VAL ASP          
SEQRES   9 A  302  ALA ILE MET LEU GLU LEU ASP ARG GLY LEU THR GLU PRO          
SEQRES  10 A  302  GLN ILE GLN VAL VAL CYS ARG GLN MET LEU GLU ALA LEU          
SEQRES  11 A  302  ASN PHE LEU HIS SER LYS ARG ILE ILE HIS ARG ASP LEU          
SEQRES  12 A  302  LYS ALA GLY ASN VAL LEU MET THR LEU GLU GLY ASP ILE          
SEQRES  13 A  302  ARG LEU ALA ASP PHE GLY VAL SER ALA LYS ASN LEU LYS          
SEQRES  14 A  302  THR LEU GLN LYS ARG ASP SER PHE ILE GLY THR PRO TYR          
SEQRES  15 A  302  TRP MET ALA PRO GLU VAL VAL MET CYS GLU THR MET LYS          
SEQRES  16 A  302  ASP THR PRO TYR ASP TYR LYS ALA ASP ILE TRP SER LEU          
SEQRES  17 A  302  GLY ILE THR LEU ILE GLU MET ALA GLN ILE GLU PRO PRO          
SEQRES  18 A  302  HIS HIS GLU LEU ASN PRO MET ARG VAL LEU LEU LYS ILE          
SEQRES  19 A  302  ALA LYS SER ASP PRO PRO THR LEU LEU THR PRO SER LYS          
SEQRES  20 A  302  TRP SER VAL GLU PHE ARG ASP PHE LEU LYS ILE ALA LEU          
SEQRES  21 A  302  ASP LYS ASN PRO GLU THR ARG PRO SER ALA ALA GLN LEU          
SEQRES  22 A  302  LEU GLU HIS PRO PHE VAL SER SER ILE THR SER ASN LYS          
SEQRES  23 A  302  ALA LEU ARG GLU LEU VAL ALA GLU ALA LYS ALA GLU VAL          
SEQRES  24 A  302  MET GLU GLU                                                  
SEQRES   1 B  302  SER MET ARG LYS SER ARG GLU TYR GLU HIS VAL ARG ARG          
SEQRES   2 B  302  ASP LEU ASP PRO ASN GLU VAL TRP GLU ILE VAL GLY GLU          
SEQRES   3 B  302  LEU GLY ASP GLY ALA PHE GLY LYS VAL TYR LYS ALA LYS          
SEQRES   4 B  302  ASN LYS GLU THR GLY ALA LEU ALA ALA ALA LYS VAL ILE          
SEQRES   5 B  302  GLU THR LYS SER GLU GLU GLU LEU GLU ASP TYR ILE VAL          
SEQRES   6 B  302  GLU ILE GLU ILE LEU ALA THR CYS ASP HIS PRO TYR ILE          
SEQRES   7 B  302  VAL LYS LEU LEU GLY ALA TYR TYR HIS ASP GLY LYS LEU          
SEQRES   8 B  302  TRP ILE MET ILE GLU PHE CYS PRO GLY GLY ALA VAL ASP          
SEQRES   9 B  302  ALA ILE MET LEU GLU LEU ASP ARG GLY LEU THR GLU PRO          
SEQRES  10 B  302  GLN ILE GLN VAL VAL CYS ARG GLN MET LEU GLU ALA LEU          
SEQRES  11 B  302  ASN PHE LEU HIS SER LYS ARG ILE ILE HIS ARG ASP LEU          
SEQRES  12 B  302  LYS ALA GLY ASN VAL LEU MET THR LEU GLU GLY ASP ILE          
SEQRES  13 B  302  ARG LEU ALA ASP PHE GLY VAL SER ALA LYS ASN LEU LYS          
SEQRES  14 B  302  THR LEU GLN LYS ARG ASP SER PHE ILE GLY THR PRO TYR          
SEQRES  15 B  302  TRP MET ALA PRO GLU VAL VAL MET CYS GLU THR MET LYS          
SEQRES  16 B  302  ASP THR PRO TYR ASP TYR LYS ALA ASP ILE TRP SER LEU          
SEQRES  17 B  302  GLY ILE THR LEU ILE GLU MET ALA GLN ILE GLU PRO PRO          
SEQRES  18 B  302  HIS HIS GLU LEU ASN PRO MET ARG VAL LEU LEU LYS ILE          
SEQRES  19 B  302  ALA LYS SER ASP PRO PRO THR LEU LEU THR PRO SER LYS          
SEQRES  20 B  302  TRP SER VAL GLU PHE ARG ASP PHE LEU LYS ILE ALA LEU          
SEQRES  21 B  302  ASP LYS ASN PRO GLU THR ARG PRO SER ALA ALA GLN LEU          
SEQRES  22 B  302  LEU GLU HIS PRO PHE VAL SER SER ILE THR SER ASN LYS          
SEQRES  23 B  302  ALA LEU ARG GLU LEU VAL ALA GLU ALA LYS ALA GLU VAL          
SEQRES  24 B  302  MET GLU GLU                                                  
HET    R09  A 500      35                                                       
HET    R09  B 500      35                                                       
HETNAM     R09 4-{5-(6-METHOXYNAPHTHALEN-2-YL)-1-METHYL-2-[2-METHYL-4-          
HETNAM   2 R09  (METHYLSULFONYL)PHENYL]-1H-IMIDAZOL-4-YL}PYRIDINE               
FORMUL   3  R09    2(C28 H25 N3 O3 S)                                           
FORMUL   5  HOH   *16(H2 O)                                                     
HELIX    1   1 SER A   71  CYS A   88  1                                  18    
HELIX    2   2 VAL A  118  LEU A  125  1                                   8    
HELIX    3   3 THR A  130  LYS A  151  1                                  22    
HELIX    4   4 LYS A  159  GLY A  161  5                                   3    
HELIX    5   5 PHE A  176  LEU A  183  1                                   8    
HELIX    6   6 ALA A  200  THR A  212  1                                  13    
HELIX    7   7 ASP A  215  ILE A  233  1                                  19    
HELIX    8   8 ASN A  241  SER A  252  1                                  12    
HELIX    9   9 SER A  264  LEU A  275  1                                  12    
HELIX   10  10 SER A  284  LEU A  289  1                                   6    
HELIX   11  11 HIS A  291  SER A  296  1                                   6    
HELIX   12  12 ASN A  300  GLU A  316  1                                  17    
HELIX   13  13 LEU B   75  CYS B   88  1                                  14    
HELIX   14  14 VAL B  118  LEU B  125  1                                   8    
HELIX   15  15 THR B  130  LYS B  151  1                                  22    
HELIX   16  16 LYS B  159  GLY B  161  5                                   3    
HELIX   17  17 PHE B  176  GLN B  187  1                                  12    
HELIX   18  18 ALA B  200  THR B  212  1                                  13    
HELIX   19  19 ASP B  215  ILE B  233  1                                  19    
HELIX   20  20 ASN B  241  SER B  252  1                                  12    
HELIX   21  21 SER B  264  LEU B  275  1                                  12    
HELIX   22  22 SER B  284  LEU B  289  1                                   6    
HELIX   23  23 HIS B  291  SER B  296  1                                   6    
HELIX   24  24 ASN B  300  GLU B  316  1                                  17    
SHEET    1  AA 5 TRP A  36  GLU A  41  0                                        
SHEET    2  AA 5 TYR A  51  ASN A  55 -1  O  LYS A  52   N  VAL A  39           
SHEET    3  AA 5 LEU A  61  GLU A  68 -1  O  ALA A  62   N  ALA A  53           
SHEET    4  AA 5 LYS A 105  GLU A 111 -1  O  LEU A 106   N  ILE A  67           
SHEET    5  AA 5 LEU A  96  HIS A 102 -1  N  LEU A  97   O  MET A 109           
SHEET    1  AB 3 GLY A 116  ALA A 117  0                                        
SHEET    2  AB 3 VAL A 163  MET A 165 -1  N  MET A 165   O  GLY A 116           
SHEET    3  AB 3 ILE A 171  LEU A 173 -1  O  ARG A 172   N  LEU A 164           
SHEET    1  BA 5 TRP B  36  GLU B  41  0                                        
SHEET    2  BA 5 TYR B  51  ASN B  55 -1  O  LYS B  52   N  VAL B  39           
SHEET    3  BA 5 LEU B  61  LYS B  65 -1  O  ALA B  62   N  ALA B  53           
SHEET    4  BA 5 ILE B 108  GLU B 111 -1  O  ILE B 108   N  LYS B  65           
SHEET    5  BA 5 LEU B  96  ALA B  99 -1  N  LEU B  97   O  MET B 109           
SHEET    1  BB 3 GLY B 116  ALA B 117  0                                        
SHEET    2  BB 3 VAL B 163  MET B 165 -1  N  MET B 165   O  GLY B 116           
SHEET    3  BB 3 ILE B 171  LEU B 173 -1  O  ARG B 172   N  LEU B 164           
SSBOND   1 CYS A  206    CYS B  206                          1555   1565  2.54  
SITE     1 AC1  8 ALA A  63  ILE A 108  ILE A 110  PHE A 112                    
SITE     2 AC1  8 CYS A 113  ALA A 117  GLY A 161  LEU A 164                    
SITE     1 AC2  7 ALA B  63  GLU B  81  ILE B 108  ILE B 110                    
SITE     2 AC2  7 CYS B 113  GLY B 161  LEU B 164                               
CRYST1   62.040   50.250  133.710  90.00 101.16  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016119  0.000000  0.003180        0.00000                         
SCALE2      0.000000  0.019900  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007623        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system